C-X center dot center dot center dot H Contacts in Biomolecular Systems: How They Contribute to Protein-Ligand Binding Affinity
文献类型：期刊论文
| 作者 | Lu, Yunxiang1; Wang, Yong1; Xu, Zhijian1 ; Yan, Xiuhua1; Luo, Xiaoming1; Jiang, Hualiang1; Zhu, Weiliang1,2
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| 刊名 | JOURNAL OF PHYSICAL CHEMISTRY B
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| 出版日期 | 2009-09-17 |
| 卷号 | 113期号:37页码:12615-12621 |
| ISSN号 | 1520-6106 |
| DOI | 10.1021/jp906352e |
| 文献子类 | Article |
| 英文摘要 | The hydrogen bond acceptor capability of halogens has long been underappreciated in the field of biology. In this work, we have surveyed structures of protein complexes with halogenated ligands to characterize geometrical preferences of C-X center dot center dot center dot H contacts and contributions of such interactions to protein-ligand binding C, affinity. Notably, F center dot center dot center dot H interactions in biomolecules exhibit a remarkably different behavior as compared to three other kinds of X center dot center dot center dot H (X = Cl, Br, I) interactions, which has been rationalized by means of A initio calculations using simple model systems. The C-X center dot center dot center dot H contacts in biological systems are characterized as weak hydrogen bonding interactions. Furthermore, the electrophile "head on" and nucleophile "side on" interactions of halogens have been extensively investigated through the examination of interactions in protein structures and a two-layer ONIOM-based QM/MM method. In biomolecullar systems, C-X center dot center dot center dot H contacts are recognized as secondary interaction contributions to C-X center dot center dot center dot O halogen bonds that play important roles in conferring specificity and affinity for halogenated ligands. The results presented here are within the context of their potential applications in drug design, including relevance to the development of accurate force fields for halogens. |
| WOS关键词 | HALOGEN BONDING INTERACTIONS ; SIGMA-HOLE ; INTERMOLECULAR INTERACTIONS ; ACTIVE-SITE ; CATION-PI ; MOLECULAR-INTERACTIONS ; OXIDATIVE ADDITION ; CH/PI INTERACTIONS ; CRYSTAL-STRUCTURE ; HYDROGEN-BONDS |
| 资助项目 | Hi-Tech Research and Development Program of China[2006AA02Z336] ; Postdoctoral Science Foundation of China[20080440664] ; CAS[KSCX2-YW-R-18] |
| WOS研究方向 | Chemistry |
| 语种 | 英语 |
| WOS记录号 | WOS:000269655700021 |
| 出版者 | AMER CHEMICAL SOC |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/279128]  |
| 专题 | 药物发现与设计中心 |
| 通讯作者 | Zhu, Weiliang |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Mat Med, Drug Discovery & Design Ctr, Shanghai 201203, Peoples R China; 2.E China Univ Sci & Technol, Sch Sci, Shanghai 200237, Peoples R China |
| 推荐引用方式 GB/T 7714 | Lu, Yunxiang,Wang, Yong,Xu, Zhijian,et al. C-X center dot center dot center dot H Contacts in Biomolecular Systems: How They Contribute to Protein-Ligand Binding Affinity[J]. JOURNAL OF PHYSICAL CHEMISTRY B,2009,113(37):12615-12621. |
| APA | Lu, Yunxiang.,Wang, Yong.,Xu, Zhijian.,Yan, Xiuhua.,Luo, Xiaoming.,...&Zhu, Weiliang.(2009).C-X center dot center dot center dot H Contacts in Biomolecular Systems: How They Contribute to Protein-Ligand Binding Affinity.JOURNAL OF PHYSICAL CHEMISTRY B,113(37),12615-12621. |
| MLA | Lu, Yunxiang,et al."C-X center dot center dot center dot H Contacts in Biomolecular Systems: How They Contribute to Protein-Ligand Binding Affinity".JOURNAL OF PHYSICAL CHEMISTRY B 113.37(2009):12615-12621. |
入库方式： OAI收割
来源：上海药物研究所
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